3NG2: Crystal Structure Of The Rnf4 Ring Domain Dimer

Citation:
Abstract
RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization.
PDB ID: 3NG2Download
MMDB ID: 85352
PDB Deposition Date: 2010/6/10
Updated in MMDB: 2010/10
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3NG2: dimeric; determined by author
Molecular Components in 3NG2
Label Count Molecule
Proteins (2 molecules)
2
Ring Finger Protein 4(Gene symbol: Rnf4)
Molecule annotation
Chemicals (5 molecules)
1
4
2
1
* Click molecule labels to explore molecular sequence information.

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